EC Number   |
Natural Substrates |
|---|
   2.5.1.150 | dimethylallyl diphosphate + all-trans-lycopene + H2O |
the enzyme is bifunctional. It catalyses the elongation of the C40 carotenoid all-trans-lycopene by attaching an isoprene unit at C-2 as well as the hydroxylation of the previous end of the molecule. The enzyme acts at both ends of the substrate |
| 2.5.1.150 | dimethylallyl diphosphate + all-trans-lycopene + H2O |
the enzyme is involved in the biosynthetic pathway of the C50 carotenoid bacterioruberin. The enzyme is bifunctional. It catalyses the elongation of the C40 carotenoid all-trans-lycopene by attaching an isoprene unit at C-2 as well as the hydroxylation of the previous end of the molecule. The enzyme acts at both ends of the substrate |
| 2.5.1.150 | dimethylallyl diphosphate + isopentenyldehydrorhodopin + H2O |
the enzyme is bifunctional. It catalyses the elongation of the C40 carotenoid all-trans-lycopene by attaching an isoprene unit at C-2 as well as the hydroxylation of the previous end of the molecule. The enzyme acts at both ends of the substrate |
| 2.5.1.150 | dimethylallyl diphosphate + isopentenyldehydrorhodopin + H2O |
the enzyme is involved in the biosynthetic pathway of the C50 carotenoid bacterioruberin. The enzyme is bifunctional. It catalyses the elongation of the C40 carotenoid all-trans-lycopene by attaching an isoprene unit at C-2 as well as the hydroxylation of the previous end of the molecule. The enzyme acts at both ends of the substrate |
